SCOPe 2.06: Domain d1gph22: 1gph 2:1-234

Lineage for d1gph22 (1gph 2:1-234)

1. Root: SCOPe 2.06

2. Class d: Alpha and beta proteins (a+b) [53931] (385 folds)

3. Fold d.153: Ntn hydrolase-like [56234] (2 superfamilies)
   4 layers: alpha/beta/beta/alpha; has an unusual sheet-to-sheet packing

4. Superfamily d.153.1: N-terminal nucleophile aminohydrolases (Ntn hydrolases) [56235] (8 families)
   N-terminal residue provides two catalytic groups, nucleophile and proton donor

5. Family d.153.1.1: Class II glutamine amidotransferases [56236] (6 proteins)
   has slightly different topology than other families do

6. Protein Glutamine PRPP amidotransferase, N-terminal domain [56239] (2 species)

7. Species Bacillus subtilis [TaxId:1423] [56240] (2 PDB entries)

8. Domain d1gph22: 1gph 2:1-234 [41813]
   Other proteins in same PDB: d1gph11, d1gph21, d1gph31, d1gph41
   complexed with amp, sf4

Details for d1gph22

PDB Entry: 1gph, 3 Å

PDB Description: structure of the allosteric regulatory enzyme of purine biosynthesis

PDB Compounds: (2:) glutamine phosphoribosyl-pyrophosphate amidotransferase

SCOPe Domain Sequences for d1gph22:

Sequence; same for both SEQRES and ATOM records:

>d1gph22 d.153.1.1 (2:1-234) Glutamine PRPP amidotransferase, N-terminal domain {Bacillus subtilis [TaxId: 1423]}
cgvfgiwgheeapqityyglhslqhrgqegagivatdgekltahkgqglitevfqngels
kvkgkgaighvryataggggyenvqpllfrsqnngslalahngnlvnatqlkqqlenqgs
ifqtssdtevlahlikrsghftlkdqiknslsmlkgayaflimtetemivaldpnglrpl
sigmmgdayvvasetcafdvvgatylrevepgemliindegmkserfsmninrs

Timeline for d1gph22:

• d1gph22 first appeared (with stable ids) in SCOP 1.55
  
• d1gph22 appears in SCOPe 2.05
  
• d1gph22 appears in SCOPe 2.07
  
• d1gph22 appears in the current release, SCOPe 2.08